Development of a monoclonal antibody based enzyme immunoassay method for analysis of maleic hydrazide

Harrison, Robert O.; Brimfield, Alan A.; Nelson, Jonathan D.

doi:10.1021/jf00088a029

Cited by 29 publications

(20 citation statements)

References 27 publications

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“…Methanol has a very strong positive effect on the antibody-antigen binding. Similar effects were reported by Harrison et al (1989). The use of a constant moderate amount of organic solvent in the assay can reduce assay variability by decreasing interference from lipid micelles with complex matrices as well as by reducing binding of analyte to surfaces.…”

Section: Resultssupporting

confidence: 71%

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Development of an enzyme-linked immunosorbent assay for the herbicide bentazon

Li¹,

Hammock²,

Seiber³

1991

J. Agric. Food Chem.

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Section: Resultssupporting

confidence: 71%

“…The effect of pH on Abl283 and its interactions with coating antigens (cAgl-3) and analytes were investigated according to the method of Harrison et al (1989). The results indicated that pH effects vary from system to system and that the antibody binding is generally maximal near physiological pH.…”

Section: Resultsmentioning

confidence: 99%

Development of an enzyme-linked immunosorbent assay for the herbicide bentazon

Li¹,

Hammock²,

Seiber³

1991

J. Agric. Food Chem.

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“…However, the ELISA had a LOD of 5 ng‚mL -1 , which was not sensitive enough for assay application. As a result, development efforts focused on the production of a heterologous assay since sensitivity can be improved by promoting an environment with a "biased equilibrium" in which the antisera's affinity for the compound to be detected is higher than the affinity of the antisera for the hapten conjugate (Wie and Hammock, 1984;Harrison et al, 1989a). Desired sensitivity was achieved by using fluroxypyr as the enzyme conjugate ligand.…”

Section: Resultsmentioning

confidence: 99%

Fluroxypyr- and Triclopyr-Specific Enzyme-Linked Immunosorbent Assays: Development and Quantitation in Soil and Water

and

Hall

1996

J. Agric. Food Chem.

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Enzyme-linked immunosorbent assays (ELISAs) were developed to quantitate fluroxypyr [[(4-amino-3,5-dichloro-6-fluoro-2-pyridinyl)oxy]acetic acid] and triclopyr [[(3,5,6-trichloro-2-pyridinyl)oxy]acetic acid] in soil and water. The linear working range of the fluroxypyr ELISA was from 0.1 to 10 ng‚mL -1 with a limit of detection (LOD) of 0.1 ng‚mL -1 and an IC 50 value of 1.6 ng‚mL -1 . The linear working range of the triclopyr ELISA was from 0.1 to 5 ng‚mL -1 with a LOD of 0.1 ng‚mL -1 and an IC 50 value of 1.7 ng‚mL -1 . Cross-reactivity to selected pyridine metabolites and agrochemicals was determined. Significant cross-reactivity (within the linear working range of the ELISA) using the fluroxypyr ELISA was found only to the metabolite 4-amino-3,5-dichloro-6-fluoro-2-methoxypyridine. Significant cross-reactivity using the triclopyr ELISA was found only to the auxinic herbicide 2,4,5trichlorophenoxyacetic acid (2,4,5-T). The ELISAs accurately estimated fluroxypyr and triclopyr in water at concentrations as low as 0.1 ng‚mL -1 . Analysis of two different soil types with different textures (clay loam and sandy clay loam) required cleanup procedures using filtration and solid phase extraction to accurately estimate fluroxypyr and triclopyr concentrations.

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“…Previous studies have demonstrated the value of heterologous assays in improving ELISA sensitivity for environmental compounds (Wie and Hammock, 1984;Harrison et aL, 1989). The most sensitive assays utilized antisera against the periodate antigen and either /8-exotoxin-Gior -G2-BSA or /3-exotoxin-Di-BSA as the Table III.…”

Section: Resultsmentioning

confidence: 99%

Development of an enzyme-linked immunosorbent assay for the .beta.-exotoxin of Bacillus thuringiensis

Bekheit¹,

Lucas²,

Gee³

et al. 1993

J. Agric. Food Chem.

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A competitive enzyme-linked immunosorbent assay (ELISA) was developed to quantify the amount of d-exotoxin from Bacillus thuringiensis in solution and to evaluate the ability of the antibodies to distinguish among various natural and synthetic compounds related to the d-exotoxin. The d-exotoxin was coupled to several proteins via glutaraldehyde, diazotization, and periodate procedures. The antibodies used in the assay were obtained from antisera raised against d-exotoxin linked to keyhole limpet hemocyanin, and the ELISA coating antigens consisted of d-exotoxin-bovine serum albumin conjugates. Both homologous and heterologous ELISA systems were examined. The homologous systems were not useful because the free d-exotoxin did not inhibit antibody binding to the solid phase. The heterologous systems yielded the most sensitive assays, but antisera obtained from all of the immunogens were used successfully in developing ELISAs for d-exotoxin. With these sensitive ELISAs, d-exotoxin was detected in samples of commercial formulations at levels as low as 0.1 ng/mL. A good correlation was observed when culture media was fortified with d-exotoxin and analyzed in a blind fashion with both HPLC and ELISA. These data suggest that the ELISA could be a valuable tool for detecting and quantifying d-exotoxin.

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Development of a monoclonal antibody based enzyme immunoassay method for analysis of maleic hydrazide

Cited by 29 publications

References 27 publications

Development of an enzyme-linked immunosorbent assay for the herbicide bentazon

Development of an enzyme-linked immunosorbent assay for the herbicide bentazon

Fluroxypyr- and Triclopyr-Specific Enzyme-Linked Immunosorbent Assays: Development and Quantitation in Soil and Water

Development of an enzyme-linked immunosorbent assay for the .beta.-exotoxin of Bacillus thuringiensis

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